DEN1A_HUMAN - dbPTM
DEN1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEN1A_HUMAN
UniProt AC Q8TEH3
Protein Name DENN domain-containing protein 1A {ECO:0000312|HGNC:HGNC:29324}
Gene Name DENND1A {ECO:0000312|HGNC:HGNC:29324}
Organism Homo sapiens (Human).
Sequence Length 1009
Subcellular Localization Cytoplasmic vesicle, clathrin-coated vesicle membrane
Peripheral membrane protein . Cell junction, synapse, presynaptic cell membrane . Associates to membranes via lipid-binding activity.
Protein Description Guanine nucleotide exchange factor (GEF) regulating clathrin-mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles and mediates exit from early endosomes. [PubMed: 20154091]
Protein Sequence MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEQPQPYRTLRESDSAEGDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVALKLTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIPRPAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVATPFTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQMPMGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSPALAPAPDSVEQLRKQWETFE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MGSRIKQNPE
-----CCCCCCCCCC		42.5724719451
11PhosphorylationRIKQNPETTFEVYVE
CCCCCCCCEEEEEEE		37.7324719451
24PhosphorylationVEVAYPRTGGTLSDP
EEEECCCCCCCCCCH		35.1428857561
119PhosphorylationLLNILADYTTKRQEN
HHHHHHHHCHHHHHH		15.6528509920
120PhosphorylationLNILADYTTKRQENQ
HHHHHHHCHHHHHHH		26.7928509920
121PhosphorylationNILADYTTKRQENQW
HHHHHHCHHHHHHHH		20.2828509920
173PhosphorylationIPENRNLTEYFVAVD
CCCCCCCCEEEEEEE		31.9922210691
175PhosphorylationENRNLTEYFVAVDVN
CCCCCCEEEEEEEHH		9.7122210691
267 (in isoform 6)Ubiquitination-2.02-
291PhosphorylationSLPNDVISSLKNRLK
HCCHHHHHHHHHHHH		29.4824719451
299UbiquitinationSLKNRLKKVSTTTGD
HHHHHHHHCCCCCCH		46.11-
301PhosphorylationKNRLKKVSTTTGDGV
HHHHHHCCCCCCHHH		28.9921406692
302PhosphorylationNRLKKVSTTTGDGVA
HHHHHCCCCCCHHHH		31.2221406692
303PhosphorylationRLKKVSTTTGDGVAR
HHHHCCCCCCHHHHH		22.6721406692
304PhosphorylationLKKVSTTTGDGVARA
HHHCCCCCCHHHHHH		33.1121406692
377PhosphorylationGRLDLLNSGEGFSDV
HCHHHHHCCCCCHHH		37.89-
394PhosphorylationEEINMGEYAGSDKLY
HHHCCCCCCCCCHHH		15.5517053785
397PhosphorylationNMGEYAGSDKLYHQW
CCCCCCCCCHHHHHH		24.3324719451
412PhosphorylationLSTVRKGSGAILNTV
HHHHHCCCCCCHHHH		28.2528857561
418PhosphorylationGSGAILNTVKTKANP
CCCCCHHHHHCCCCH		21.67-
421PhosphorylationAILNTVKTKANPAMK
CCHHHHHCCCCHHHH		30.9328555341
428AcetylationTKANPAMKTVYKFAK
CCCCHHHHHHHHHHH		36.6225953088
443UbiquitinationDHAKMGIKEVKNRLK
HHHHHCHHHHHHHHH		51.21-
446UbiquitinationKMGIKEVKNRLKQKD
HHCHHHHHHHHHHHH		37.12-
470PhosphorylationPEEQLPKTAPSPLVE
HHHHCCCCCCCCCCC		41.6930266825
473PhosphorylationQLPKTAPSPLVEAKD
HCCCCCCCCCCCCCC		28.5330266825
477 (in isoform 7)Phosphorylation-58.6528450419
478 (in isoform 7)Phosphorylation-17.6728450419
481 (in isoform 7)Phosphorylation-36.5528450419
487 (in isoform 6)Phosphorylation-41.3328450419
488 (in isoform 6)Phosphorylation-39.0228450419
489 (in isoform 5)Phosphorylation-27.7427251275
490 (in isoform 5)Phosphorylation-6.2724719451
491 (in isoform 6)Phosphorylation-15.6028450419
493 (in isoform 5)Phosphorylation-16.6925159151
510PhosphorylationHVVKRPKSNIAVEGR
CCCCCCCCCEEEECC		35.8330576142
519 (in isoform 2)Phosphorylation-32.4927251275
519PhosphorylationIAVEGRRTSVPSPEQ
EEEECCCCCCCCCCC		32.4923927012
520PhosphorylationAVEGRRTSVPSPEQP
EEECCCCCCCCCCCC		30.1620201521
520 (in isoform 2)Phosphorylation-30.1624719451
521 (in isoform 5)Phosphorylation-5.56-
523PhosphorylationGRRTSVPSPEQPQPY
CCCCCCCCCCCCCCC		38.6220201521
523 (in isoform 2)Phosphorylation-38.6225159151
527 (in isoform 5)Phosphorylation-35.14-
530PhosphorylationSPEQPQPYRTLRESD
CCCCCCCCCCCCCCC		15.8123927012
532PhosphorylationEQPQPYRTLRESDSA
CCCCCCCCCCCCCCC		25.0723911959
536PhosphorylationPYRTLRESDSAEGDE
CCCCCCCCCCCCCCC		30.3623401153
537 (in isoform 7)Phosphorylation-47.3025159151
538PhosphorylationRTLRESDSAEGDEAE
CCCCCCCCCCCCCCC		37.1823927012
546PhosphorylationAEGDEAESPEQQVRK
CCCCCCCCHHHHHHH		40.5629255136
547 (in isoform 6)Phosphorylation-34.6125159151
551 (in isoform 2)Phosphorylation-9.22-
553UbiquitinationSPEQQVRKSTGPVPA
CHHHHHHHCCCCCCC		54.21-
554PhosphorylationPEQQVRKSTGPVPAP
HHHHHHHCCCCCCCC		28.2125159151
555PhosphorylationEQQVRKSTGPVPAPP
HHHHHHCCCCCCCCC		48.8421815630
557 (in isoform 2)Phosphorylation-29.07-
567PhosphorylationAPPDRAASIDLLEDV
CCCCHHHHHHHHHHH		18.6927732954
591UbiquitinationLQPLGQAKSLEDLRA
HHHHHCCCCHHHHCC		47.92-
592PhosphorylationQPLGQAKSLEDLRAP
HHHHCCCCHHHHCCC		39.7522167270
608PhosphorylationDLREQPGTFDYQRLD
HHHCCCCCCCCCEEE		21.7326657352
611PhosphorylationEQPGTFDYQRLDLGG
CCCCCCCCCEEECCC		7.4326657352
619PhosphorylationQRLDLGGSERSRGVT
CEEECCCCCCCCCEE		28.2123401153
640PhosphorylationHPYNKLWSLGQDDMA
CCCHHHHHCCCCCCC		32.8128464451
650PhosphorylationQDDMAIPSKPPAASP
CCCCCCCCCCCCCCC		52.2428464451
656PhosphorylationPSKPPAASPEKPSAL
CCCCCCCCCCCCCHH		35.3825159151
661PhosphorylationAASPEKPSALLGNSL
CCCCCCCCHHHCCCC		42.4928450419
667PhosphorylationPSALLGNSLALPRRP
CCHHHCCCCCCCCCC		17.1426074081
679PhosphorylationRRPQNRDSILNPSDK
CCCCCCCCCCCCCCC		26.2428555341
684PhosphorylationRDSILNPSDKEEVPT
CCCCCCCCCCCCCCC		61.31-
691PhosphorylationSDKEEVPTPTLGSIT
CCCCCCCCCCCCEEE		33.8028555341
698PhosphorylationTPTLGSITIPRPQGR
CCCCCEEEECCCCCC		26.9924719451
707PhosphorylationPRPQGRKTPELGIVP
CCCCCCCCCCCCCCC		22.1930266825
723AcetylationPPIPRPAKLQAAGAA
CCCCCCHHHHHHHHH		43.7625953088
749PhosphorylationRDRRAALSPGLLPGV
HHHHHHCCCCCCCCC		16.5214702039
800PhosphorylationWSGSTLPSRPATPNV
CCCCCCCCCCCCCCC		54.7526074081
804PhosphorylationTLPSRPATPNVATPF
CCCCCCCCCCCCCCC		20.3426074081
883PhosphorylationGFCAPHRSQPNLSAL
CCCCCCCCCCCCHHH		47.1328348404
891PhosphorylationQPNLSALSMPNLFGQ
CCCCHHHCCCCCCCC		31.7326074081
903PhosphorylationFGQMPMGTHTSPLQP
CCCCCCCCCCCCCCC		18.7426074081
905PhosphorylationQMPMGTHTSPLQPLG
CCCCCCCCCCCCCCC		31.7026074081
906PhosphorylationMPMGTHTSPLQPLGP
CCCCCCCCCCCCCCC		18.9326074081
923PhosphorylationVAPSRIRTLPLARSS
CCCHHHCCHHHHHHH		30.2930266825
961PhosphorylationPPQGLEPTLQPSAPQ
CCCCCCCCCCCCCCH		28.7526074081
965PhosphorylationLEPTLQPSAPQQARD
CCCCCCCCCCHHHCC		39.3526074081
981PhosphorylationFEDLLQKTKQDVSPS
HHHHHHHHCCCCCCC		22.4526270265
986PhosphorylationQKTKQDVSPSPALAP
HHHCCCCCCCCCCCC		28.1325159151
988PhosphorylationTKQDVSPSPALAPAP
HCCCCCCCCCCCCCC		18.4621815630
997PhosphorylationALAPAPDSVEQLRKQ
CCCCCCCHHHHHHHH		26.8825159151
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DEN1A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEN1A_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DEN1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
CING_HUMANCGNphysical
27173435
MAST3_HUMANMAST3physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
ZN638_HUMANZNF638physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
CDK16_HUMANCDK16physical
27173435
HDAC4_HUMANHDAC4physical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
NF1_HUMANNF1physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
LPIN3_HUMANLPIN3physical
27173435
FA53C_HUMANFAM53Cphysical
27173435
CBY1_HUMANCBY1physical
27173435
NADK_HUMANNADKphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
MPIP3_HUMANCDC25Cphysical
27173435
TIAM1_HUMANTIAM1physical
27173435
M3K21_HUMANKIAA1804physical
27173435
CAMP2_HUMANCAMSAP2physical
27173435
NGAP_HUMANRASAL2physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
MELK_HUMANMELKphysical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
TBC25_HUMANTBC1D25physical
27173435
NAV1_HUMANNAV1physical
27173435
TANC2_HUMANTANC2physical
27173435
RPTOR_HUMANRPTORphysical
27173435
RGPS2_HUMANRALGPS2physical
27173435
DEP1B_HUMANDEPDC1Bphysical
27173435
STA13_HUMANSTARD13physical
27173435
OSBL6_HUMANOSBPL6physical
27173435
HDAC7_HUMANHDAC7physical
27173435
AFAD_HUMANMLLT4physical
27173435
LARP1_HUMANLARP1physical
27173435
PKHA5_HUMANPLEKHA5physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
KIF1B_HUMANKIF1Bphysical
27173435
INP5E_HUMANINPP5Ephysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DEN1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520; SER-523; SER-538AND SER-546, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-519; SER-520; SER-523;SER-536; SER-538; SER-546 AND SER-592, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520 AND SER-523, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-394, AND MASSSPECTROMETRY.

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